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Protein

Transcription elongation factor A protein-like 1

Gene

TCEAL1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

May be involved in transcriptional regulation. Modulates various viral and cellular promoters in a promoter context-dependent manner. For example, transcription from the FOS promoter is increased, while Rous sarcoma virus (RSV) long terminal repeat (LTR) promoter activity is repressed. Does not bind DNA directly.

GO - Molecular functioni

  • transcription factor activity, sequence-specific DNA binding Source: ProtInc
  • WW domain binding Source: GO_Central

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Transcription, Transcription regulation

Names & Taxonomyi

Protein namesi
Recommended name:
Transcription elongation factor A protein-like 1
Short name:
TCEA-like protein 1
Alternative name(s):
Nuclear phosphoprotein p21/SIIR
Transcription elongation factor S-II protein-like 1
Gene namesi
Name:TCEAL1
Synonyms:SIIR
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome X

Organism-specific databases

HGNCiHGNC:11616. TCEAL1.

Subcellular locationi

GO - Cellular componenti

  • nucleoplasm Source: HPA
  • nucleus Source: ProtInc
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi31 – 322SS → AA: Slight decrease of transcriptional repression. 1 Publication
Mutagenesisi36 – 372SS → AA: Loss of transcriptional repression. 1 Publication
Mutagenesisi41 – 422SS → AA: No effect on transcriptional repression. 1 Publication
Mutagenesisi47 – 482SS → AA: Slight decrease of transcriptional repression. 1 Publication

Organism-specific databases

PharmGKBiPA36375.

Polymorphism and mutation databases

BioMutaiTCEAL1.
DMDMi108935936.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 157157Transcription elongation factor A protein-like 1PRO_0000239203Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei31 – 311Phosphoserine1 Publication
Modified residuei32 – 321Phosphoserine1 Publication
Modified residuei36 – 361Phosphoserine1 Publication
Modified residuei37 – 371Phosphoserine1 Publication
Modified residuei41 – 411Phosphoserine1 Publication
Modified residuei42 – 421Phosphoserine1 Publication
Modified residuei47 – 471Phosphoserine1 Publication
Modified residuei48 – 481Phosphoserine1 Publication
Isoform 2 (identifier: Q15170-2)
Modified residuei28 – 281PhosphoserineCombined sources

Post-translational modificationi

Phosphorylation of Ser-36 and Ser-37 is critical for transcriptional repression.1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiQ15170.
MaxQBiQ15170.
PRIDEiQ15170.

PTM databases

iPTMnetiQ15170.
PhosphoSiteiQ15170.

Expressioni

Tissue specificityi

Expressed in all tissues examined. Highly expressed in heart, ovary, prostate and skeletal muscle. Moderately expressed in brain, placenta, testis and small intestine. Weakly expressed in lung, liver and spleen. Expressed in several cancer cell lines.1 Publication

Gene expression databases

BgeeiQ15170.
CleanExiHS_TCEAL1.
GenevisibleiQ15170. HS.

Organism-specific databases

HPAiHPA057345.

Interactioni

GO - Molecular functioni

Protein-protein interaction databases

BioGridi114745. 48 interactions.
IntActiQ15170. 17 interactions.

Structurei

3D structure databases

ProteinModelPortaliQ15170.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi15 – 7258Arg/Ser-richAdd
BLAST

Sequence similaritiesi

Belongs to the TFS-II family. TFA subfamily.Curated

Phylogenomic databases

GeneTreeiENSGT00730000111084.
HOGENOMiHOG000231344.
HOVERGENiHBG094029.
InParanoidiQ15170.
OMAiERPPMEQ.
OrthoDBiEOG757D0N.
PhylomeDBiQ15170.
TreeFamiTF336871.

Family and domain databases

InterProiIPR010370. TCEAL1.
IPR021156. TF_A-like/BEX-like.
[Graphical view]
PANTHERiPTHR14754:SF12. PTHR14754:SF12. 1 hit.
PfamiPF04538. BEX. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q15170-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MDKPRKENEE EPQSRPRPMR RGLRWSTLPK SSPPRSSLRR SSPRRRSSFL
60 70 80 90 100
RSSCLSSCLR CSSRRTPSAG LSRKDLFEGR PPMEQPPCGV GKHKLEEGSF
110 120 130 140 150
KERLARSRPQ FRGDIHGRNL SNEEMIQAAD ELEEMKRVRN KLMIMHWKAK

RSRPYPI
Length:157
Mass (Da):18,354
Last modified:May 30, 2006 - v2
Checksum:i09D86B3735283B27
GO
Isoform 2 (identifier: Q15170-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     15-69: RPRPMRRGLR...RCSSRRTPSA → APKTDEERPP...LLSEERPPQE

Show »
Length:159
Mass (Da):18,641
Checksum:iFB45224005BA6B5A
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti79 – 791G → V (PubMed:8206389).Curated
Sequence conflicti79 – 791G → V (PubMed:10051408).Curated
Sequence conflicti94 – 941K → N (PubMed:8206389).Curated
Sequence conflicti94 – 941K → N (PubMed:10051408).Curated
Sequence conflicti99 – 991S → I (PubMed:8206389).Curated
Sequence conflicti99 – 991S → I (PubMed:10051408).Curated
Sequence conflicti148 – 1481K → R (PubMed:8206389).Curated
Sequence conflicti148 – 1481K → R (PubMed:10051408).Curated
Sequence conflicti152 – 1532SR → GG (PubMed:8206389).Curated
Sequence conflicti152 – 1532SR → GG (PubMed:10051408).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti5 – 51R → C.
Corresponds to variant rs34421776 [ dbSNP | Ensembl ].
VAR_057270

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei15 – 6955RPRPM…RTPSA → APKTDEERPPVEHSPEKQSP EEQSSEEQSSEEEFFPEELL PELLPEMLLSEERPPQE in isoform 2. 1 PublicationVSP_019108Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M99701 mRNA. Translation: AAA60149.1.
AF095906 Genomic DNA. Translation: AAD17840.1.
AL049610 Genomic DNA. Translation: CAB55700.1.
BC000809 mRNA. Translation: AAH00809.1.
CCDSiCCDS35358.1. [Q15170-2]
PIRiI53785.
RefSeqiNP_001006640.1. NM_001006639.1. [Q15170-2]
NP_001006641.1. NM_001006640.1. [Q15170-2]
NP_004771.2. NM_004780.2. [Q15170-2]
UniGeneiHs.95243.

Genome annotation databases

EnsembliENST00000372624; ENSP00000361707; ENSG00000172465. [Q15170-2]
ENST00000372625; ENSP00000361708; ENSG00000172465. [Q15170-2]
ENST00000372626; ENSP00000361709; ENSG00000172465. [Q15170-2]
GeneIDi9338.
KEGGihsa:9338.
UCSCiuc004eks.4. human. [Q15170-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M99701 mRNA. Translation: AAA60149.1.
AF095906 Genomic DNA. Translation: AAD17840.1.
AL049610 Genomic DNA. Translation: CAB55700.1.
BC000809 mRNA. Translation: AAH00809.1.
CCDSiCCDS35358.1. [Q15170-2]
PIRiI53785.
RefSeqiNP_001006640.1. NM_001006639.1. [Q15170-2]
NP_001006641.1. NM_001006640.1. [Q15170-2]
NP_004771.2. NM_004780.2. [Q15170-2]
UniGeneiHs.95243.

3D structure databases

ProteinModelPortaliQ15170.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi114745. 48 interactions.
IntActiQ15170. 17 interactions.

PTM databases

iPTMnetiQ15170.
PhosphoSiteiQ15170.

Polymorphism and mutation databases

BioMutaiTCEAL1.
DMDMi108935936.

Proteomic databases

EPDiQ15170.
MaxQBiQ15170.
PRIDEiQ15170.

Protocols and materials databases

DNASUi9338.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000372624; ENSP00000361707; ENSG00000172465. [Q15170-2]
ENST00000372625; ENSP00000361708; ENSG00000172465. [Q15170-2]
ENST00000372626; ENSP00000361709; ENSG00000172465. [Q15170-2]
GeneIDi9338.
KEGGihsa:9338.
UCSCiuc004eks.4. human. [Q15170-1]

Organism-specific databases

CTDi9338.
GeneCardsiTCEAL1.
HGNCiHGNC:11616. TCEAL1.
HPAiHPA057345.
MIMi300237. gene.
neXtProtiNX_Q15170.
PharmGKBiPA36375.
GenAtlasiSearch...

Phylogenomic databases

GeneTreeiENSGT00730000111084.
HOGENOMiHOG000231344.
HOVERGENiHBG094029.
InParanoidiQ15170.
OMAiERPPMEQ.
OrthoDBiEOG757D0N.
PhylomeDBiQ15170.
TreeFamiTF336871.

Miscellaneous databases

GeneWikiiTCEAL1.
GenomeRNAii9338.
PROiQ15170.
SOURCEiSearch...

Gene expression databases

BgeeiQ15170.
CleanExiHS_TCEAL1.
GenevisibleiQ15170. HS.

Family and domain databases

InterProiIPR010370. TCEAL1.
IPR021156. TF_A-like/BEX-like.
[Graphical view]
PANTHERiPTHR14754:SF12. PTHR14754:SF12. 1 hit.
PfamiPF04538. BEX. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "A HeLa-cell-encoded p21 is homologous to transcription elongation factor SII."
    Yeh C.-H., Shatkin A.J.
    Gene 143:285-287(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  2. "Genomic structure and chromosomal localization of TCEAL1, a human gene encoding the nuclear phosphoprotein p21/SIIR."
    Pillutla R.C., Shimamoto A., Furuichi Y., Shatkin A.J.
    Genomics 56:217-220(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], TISSUE SPECIFICITY.
    Tissue: Placenta.
  3. "The DNA sequence of the human X chromosome."
    Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D., Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C.
    , Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S., Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S., Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D., Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H., McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K., Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D., Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R., Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A., Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F., Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S., Rogers J., Bentley D.R.
    Nature 434:325-337(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
    Tissue: Placenta.
  5. "The Ser36-Ser37 pair in HeLa nuclear protein p21/SIIR mediates Ser/Thr phosphorylation and is essential for Rous sarcoma virus long terminal repeat repression."
    Yeh C.-H., Zong W.-X., Shatkin A.J.
    J. Biol. Chem. 270:25313-25315(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT SER-31; SER-32; SER-36; SER-37; SER-41; SER-42; SER-47 AND SER-48, MUTAGENESIS OF 31-SER-SER-32; 36-SER-SER-37; 41-SER-SER-42 AND 47-SER-SER-48.
  6. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
    Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
    Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-28 (ISOFORM 2), IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  7. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiTCAL1_HUMAN
AccessioniPrimary (citable) accession number: Q15170
Secondary accession number(s): Q9UJQ9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 30, 2006
Last sequence update: May 30, 2006
Last modified: June 8, 2016
This is version 116 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome X
    Human chromosome X: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.